Palladin is a novel binding partner of ILKAP in eukaryotic cells |
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| Authors: | Zhou Wang Cui Shusen Han Shuhai Cheng Baiqi Zheng Yu Zhang Yingjiu |
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| Affiliation: | aKey Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun, PR China;bChina–Japan Union Hospital of Jilin University, Changchun, PR China;cThe First Affiliated Hospital of Jilin University, Changchun, PR China |
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| Abstract: | Palladin was a novel binding partner of ILKAP in eukaryotic cells. Palladin’s C-terminal fragment including only its last three Ig domains (residues 710–1106) and the PP2C domain of ILKAP (residues 108–392) were necessary and sufficient for their interaction. The biological significance of the interaction between palladin and ILKAP was that palladin recruited the cytoplasmic ILKAP to initiate ILKAP-induced apoptosis. Our results suggested that palladin played a specific role in modulating the subcellular localization of the cytoplasmic ILKAP and promoting the ILKAP-induced apoptosis. |
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| Keywords: | Abbreviations: ILKAP, integrin-linked kinase-associated phosphatase ILK, integrin-linked kinase DMEM, Dulbecco&rsquo s modified Eagle&rsquo s medium |
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